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Yorodumi- PDB-1dvx: CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dvx | ||||||
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Title | CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH DICLOFENAC | ||||||
Components | TRANSTHYRETIN | ||||||
Keywords | HORMONE/GROWTH FACTOR / THYROXINE TRANSPORT / SIGNALING PROTEIN / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation ...Retinoid cycle disease events / The canonical retinoid cycle in rods (twilight vision) / thyroid hormone binding / purine nucleobase metabolic process / Non-integrin membrane-ECM interactions / Retinoid metabolism and transport / hormone activity / azurophil granule lumen / Amyloid fiber formation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Klabunde, T. / Petrassi, H.M. / Oza, V.B. / Kelly, J.W. / Sacchettini, J.C. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2000 Title: Rational design of potent human transthyretin amyloid disease inhibitors. Authors: Klabunde, T. / Petrassi, H.M. / Oza, V.B. / Raman, P. / Kelly, J.W. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dvx.cif.gz | 54.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dvx.ent.gz | 43.9 KB | Display | PDB format |
PDBx/mmJSON format | 1dvx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dvx_validation.pdf.gz | 504 KB | Display | wwPDB validaton report |
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Full document | 1dvx_full_validation.pdf.gz | 509.1 KB | Display | |
Data in XML | 1dvx_validation.xml.gz | 6.7 KB | Display | |
Data in CIF | 1dvx_validation.cif.gz | 9.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dv/1dvx ftp://data.pdbj.org/pub/pdb/validation_reports/dv/1dvx | HTTPS FTP |
-Related structure data
Related structure data | 1dvqC 1dvsC 1dvtC 1dvuC 1dvyC 1dvzC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is a tetramer constructed from the homodimer (chain A and B) and a symmetry mate generated by the two-fold |
-Components
#1: Protein | Mass: 13420.968 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P02766 #2: Chemical | ChemComp-DIF / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.65 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: potassium chloride potassium phosphate ammonium sulfate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Oct 10, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. all: 16154 / Num. obs: 16154 / % possible obs: 97.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.48 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 9.9 |
Reflection shell | Resolution: 1.9→2 Å / Rmerge(I) obs: 0.217 / % possible all: 90.5 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / Num. measured all: 72331 |
Reflection shell | *PLUS % possible obs: 90.5 % |
-Processing
Software |
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Refinement | Resolution: 2→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber Details: The structure contains two diclofenac molecules that bind in each of two independent binding sites of the tetramer. Since the binding is along the 2-fold crystallographic axis, an occupancy ...Details: The structure contains two diclofenac molecules that bind in each of two independent binding sites of the tetramer. Since the binding is along the 2-fold crystallographic axis, an occupancy of 0.5 corresponds to saturation of each of the binding sites. Binding of diclofenac in two symmetry-related binding modes induces alternate side chain conformations for the protein residues Val17, Ser117, and Thr119.
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.192 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |